8WWS
Crystal structure of cis-epoxysuccinate hydrolase from Klebsiella oxytoca with L(+)-tartaric acid
Summary for 8WWS
| Entry DOI | 10.2210/pdb8wws/pdb |
| Descriptor | (S)-2-haloacid dehalogenase, L(+)-TARTARIC ACID, 1,2-ETHANEDIOL, ... (6 entities in total) |
| Functional Keywords | cis-epoxysuccinate hydrolase, hydrolase |
| Biological source | Klebsiella oxytoca |
| Total number of polymer chains | 4 |
| Total formula weight | 124017.37 |
| Authors | Han, Y.,Kong, X.D.,Li, J.,Xu, J.H. (deposition date: 2023-10-26, release date: 2024-06-12, Last modification date: 2024-07-03) |
| Primary citation | Han, Y.,Luo, Y.,Ma, B.D.,Li, J.,Xu, J.H.,Kong, X.D. Structural Insights of a cis -Epoxysuccinate Hydrolase Facilitate the Development of Robust Biocatalysts for the Production of l-(+)-Tartrate. Biochemistry, 63:1578-1587, 2024 Cited by PubMed Abstract: l-(+)-Tartaric acid plays important roles in various industries, including pharmaceuticals, foods, and chemicals. -Epoxysuccinate hydrolases (CESHs) are crucial for converting -epoxysuccinate to l-(+)-tartrate in the industrial production process. There is, however, a lack of detailed structural and mechanistic information on CESHs, limiting the discovery and engineering of these industrially relevant enzymes. In this study, we report the crystal structures of CESH and CESH-l-(+)-tartrate complex. These structures reveal the key amino acids of the active pocket and the catalytic triad residues and elucidate a dynamic catalytic process involving conformational changes of the active site. Leveraging the structural insights, we identified a robust CESH (550 ± 20 U·mg) with sustained catalytic activity even at a 3 M substrate concentration. After six batches of transformation, immobilized cells with overexpressed CESH maintained 69% of their initial activity, affording an overall productivity of 200 g/L/h. These results provide valuable insights into the development of high-efficiency CESHs and the optimization of biotransformation processes for industrial uses. PubMed: 38803051DOI: 10.1021/acs.biochem.4c00141 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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